1yk9: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND=  
|LIGAND=  
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] </span>
|GENE= Rv1625c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|GENE= Rv1625c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00211 Guanylate_cyc]</span>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yk9 OCA], [http://www.ebi.ac.uk/pdbsum/1yk9 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1yk9 RCSB]</span>
}}
}}


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[[Category: tbsgc]]
[[Category: tbsgc]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:58 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:15:16 2008''

Revision as of 07:15, 26 March 2008

File:1yk9.gif


PDB ID 1yk9

Drag the structure with the mouse to rotate
, resolution 2.70Å
Gene: Rv1625c (Mycobacterium tuberculosis)
Activity: Adenylate cyclase, with EC number 4.6.1.1
Domains: Guanylate_cyc
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c


OverviewOverview

The Rv1625c Class III adenylyl cyclase from Mycobacterium tuberculosis is a homodimeric enzyme with two catalytic centers at the dimer interface, and shows sequence similarity with the mammalian adenylyl and guanylyl cyclases. Mutation of the substrate-specifying residues in the catalytic domain of Rv1625c, either independently or together, to those present in guanylyl cyclases not only failed to confer guanylyl cyclase activity to the protein, but also severely abrogated the adenylyl cyclase activity of the enzyme. Biochemical analysis revealed alterations in the behavior of the mutants on ion-exchange chromatography, indicating differences in the surface-exposed charge upon mutation of substrate-specifying residues. The mutant proteins showed alterations in oligomeric status as compared to the wild-type enzyme, and differing abilities to heterodimerize with the wild-type protein. The crystal structure of a mutant has been solved to a resolution of 2.7A. On the basis of the structure, and additional biochemical studies, we provide possible reasons for the altered properties of the mutant proteins, as well as highlight unique structural features of the Rv1625c adenylyl cyclase.

About this StructureAbout this Structure

1YK9 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis., Ketkar AD, Shenoy AR, Ramagopal UA, Visweswariah SS, Suguna K, J Mol Biol. 2006 Mar 3;356(4):904-16. Epub 2005 Dec 22. PMID:16403515

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